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High salt-resistance antibacterial peptide and method for producing the same

a high salt resistance, antibacterial technology, applied in the direction of antibacterial agents, peptides/protein ingredients, peptides, etc., can solve the problems of defective protection function of antibacterial peptides, and achieve the effect of increasing the width and/or the length, and increasing the salt resistance of an antibacterial peptid

Active Publication Date: 2013-05-02
NATIONAL TSING HUA UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The present invention provides a way to make an antibacterial peptide that is resistant to high salt levels. This is accomplished by changing the width and length of a specific part of the peptide's structure called the hydrophobic terminal. The method can help evaluate the effectiveness of the antibacterial peptide in high salt conditions.

Problems solved by technology

However, in mammals, it has been proved that this kind of antibacterial peptide performs defective protection function in defective bacterial killing of patients and mice with Cystic fibrosis.

Method used

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  • High salt-resistance antibacterial peptide and method for producing the same
  • High salt-resistance antibacterial peptide and method for producing the same
  • High salt-resistance antibacterial peptide and method for producing the same

Examples

Experimental program
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Effect test

example 1

Preparation of Phe-P113, Nal-P113 and Bip-P113

[0039]The Phe-P113, Nal-P113 and Bip-P113 is purchased from SynBioSci. Corp. (commercialized artificial peptide) and the purity is exceed 95% which is tested by MALDI-TOF.

[0040]As shown in FIG. 2, the histidine of the His4(4), His5(5) and His12(6) of hydrophobic terminal (11) in P113 is substituted by Phe(Phenylalanine, 2-Nal 2-Naphthylalanine and Bip[β-(4,4′-biphenyl)alanine during the synthesis. Wherein the Phe-P113 which is substituted by Phe is control group, and the Nal-P113 and Bip-P113 which is substituted by 2-Nal and Bip relatively is experimental group.

[0041]The peptide structure is shown as FIG. 3, this is a mimic of Nal-P113 attached on the surface of a microbe and is a lateral sectional view of 3D structure of lateral structure (3) of Nal-P113 α-helix with longitudinal structure of P113 a-helix (31). The lateral line is cell membrane (10) of the surface of the microbe, and above this line is outside (101) of the microbe so i...

example 2

The Antibacterial Ability of Phe-P113, Nal-P113 and Bip-P113

[0042]For testing the antibacterial ability of Phe-P113, Nal-P113 and Bip-P113 in different salt concentration, we use Antibacterial activity assay to perform the test. Three bacteria strains are used: Eschericha coli strains (ATCC 25922), Staphylococcus aureus strains (ATCC 25923, 29213 and 19636, methicillin-resistant) and Pseudomonas aeruginosa strains (ATCC 27853 and 9027, ampicillin-resistant).

[0043]The microdilution method of National Committee for Clinical Laboratory Standards (NCCLS) is used to evaluate ‘The minimal inhibition concentration (MIC)’. The minimum concentration that can inhibit 90% or more microbes is the ‘minimal inhibition concentration’.

[0044]In the microdilution method, the 1 μl peptide solution (The concentration is between the range of 5000 μg / ml to 78.1 μg / ml) and the 99 μl inoculums (5×10̂5 CFU / ml) is mixed incubated in 96-well culture dish coated with polyethylene under 37° C. for 16 hr. Then e...

example 3

Evaluation the Antibacterial Ability of Phe-P113, Nal-P113 and Bip-P113 in Different Salt Concentration

[0046]Then, evaluated the antibacterial ability of Phe-P113 (represented as Phe), Nal-P113 (represented as Nal) and Bip-P113 (represented as Bip) in different salt concentration. The result is showed as TABLE 2:

TABLE 2Evaluation the antibacterial ability of Phe-P113, Nal-P113 andBip-P113 in different salt concentrationBacteria strainsATCC 25922ATCC 25923ATCC 29213ATCC 19636ATCC 27853ATCC 9027ControlP11312.512.512.5502512.5groupPhe12.56.256.25252525Nal3.1251.561.566.251.563.125Bip6.253.1253.1256.253.1253.125NaCl 50 mMP113505050505050Phe5012.512.55050>50Nal3.1251.561.5612.51.566.25Bip6.253.1253.1256.253.1253.125100 mMP113505050505050Phe>505050>5050>50Nal12.53.1253.1252512.550Bip6.256.253.1256.256.256.25200 mMP113>50>50>50>50>50>50Phe>50>50>50>50>50>50Nal2512.56.25505050Bip12.56.253.12512.56.256.25300 mMP113>50>50>50>50>50>50Phe>50>50>50>50>50>50Nal50502550>50>50Bip12.52512.512.512.55...

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Abstract

The present invention is related to a high salt-resistance antibacterial peptide by increasing width of side chain of amino acids and / or increasing length of side chain of amino acids in the antibacterial peptide; and a method for increasing salt-resistance of antibacterial peptide by increasing width of side chain and / or increasing length of side chain in the antibacterial peptide.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS[0001]This Non-provisional application claims priority under 35 U.S.C. §119(a) on Patent Application No(s). [100138970] filed in Taiwan, Republic of China [10 26, 2011], the entire contents of which are hereby incorporated by reference.FIELD OF THE INVENTION[0002]The present invention relates to a high salt-resistance antibacterial peptide and a method for increasing the salt resistance of an antibacterial peptide, especially related to increase the salt-resistance by increasing the width of a side chain of a hydrophobic terminal in an amino acid and / or by increasing the length of a side chain of a hydrophobic terminal in an amino acid.BACKGROUND OF THE INVENTION[0003]As for the generating of drug-resistance microorganism by traditional antibiotics, many research focused on new therapeutic reagent, including many antibiotic peptides generated from animals. Antimicrobial peptides play important roles in the host innate defense mechanism by inter...

Claims

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Application Information

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IPC IPC(8): C07K7/08
CPCC07K7/08A61P31/04
Inventor CHENG, JYA-WEIYU, HUI-YUANCHENG, HSI-TSUNGHUANG, KUO-CHUN
Owner NATIONAL TSING HUA UNIVERSITY